The domain within your query sequence starts at position 35 and ends at position 98; the E-value for the ADH_N domain shown below is 1.5e-16.

SHQVLIKVHACGVNPVETYIRSGAYSRKPALPYTPGSDVAGIIESVGDKVSAFKKGDRVF
CYS

ADH_N

ADH_N
PFAM accession number:PF08240
Interpro abstract (IPR013154):

This is the catalytic domain of alcohol dehydrogenases ( EC 1.1.1.1 ). Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure; a name derived from the superfamily of proteins with a GroES fold. Proteins with a GroES fold structure have a highly conserved hydrophobic core and a glycyl-aspartate dipeptide which is thought to maintain the fold [ (PUBMED:10556240) (PUBMED:8804825) ].

GO process:oxidation-reduction process (GO:0055114)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ADH_N